Evidence map›Paper›PMID 39891817›Full record

ArticleMolecular neurobiology2025

Involvement of CRMP2 Phosphorylation in Amyloid Beta-induced Tau Phosphorylation of Hippocampal Neurons in Alzheimer's Disease Mouse Model.

Daisuke Noguchi, Naoto Watamura, Miyu Nikkuni, Takaomi C Saido, Yoshio Goshima, Toshio Ohshima

Abstract read
In one paragraph

Article in Molecular neurobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Daisuke NoguchiDepartment of Life Science and Medical Bioscience, Laboratory for Molecular Brain Science, Waseda University, 2-2 Wakamatsu-Cho, Shinjuku-Ku, Tokyo, 162-8480, Japan.
Naoto WatamuraDepartment of Life Science and Medical Bioscience, Laboratory for Molecular Brain Science, Waseda University, 2-2 Wakamatsu-Cho, Shinjuku-Ku, Tokyo, 162-8480, Japan.
Miyu NikkuniDepartment of Life Science and Medical Bioscience, Laboratory for Molecular Brain Science, Waseda University, 2-2 Wakamatsu-Cho, Shinjuku-Ku, Tokyo, 162-8480, Japan.
Takaomi C SaidoLaboratory for Proteolytic Neuroscience, RIKEN Center for Brain Science, 2-1 Hirosawa, Wako-shi, Saitama, 351-0198, Japan.
Yoshio GoshimaDepartment of Molecular Pharmacology and Neurobiology, Yokohama City University Graduate School of Medicine, Yokohama, 236-0004, Japan.
Toshio OhshimaDepartment of Life Science and Medical Bioscience, Laboratory for Molecular Brain Science, Waseda University, 2-2 Wakamatsu-Cho, Shinjuku-Ku, Tokyo, 162-8480, Japan. ohshima@waseda.jp.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is the most common form of dementia, characterized by amyloid-β (Aβ) deposition and the formation of neurofibrillary tangles composed of hyperphosphorylated tau. Collapsin response mediator protein 2 (CRMP2), a microtubule (MT)-binding protein, regulates MT dynamics and is phosphorylated at Ser522 by cyclin-dependent kinase 5. Previous studies have shown increased CRMP2 phosphorylation at Ser522 (CRMP2-pSer522) in early AD stages and AD mouse models, where it colocalizes with phosphorylated tau. However, the role of CRMP-pSer522 in AD pathology remains unclear. In this study, we generated double transgenic mice by crossing tau Tg (PS19) mice and CRMP2 S522A knock-in (CRMP2KI) mice, in which S522 of CRMP2 was replaced with alanine to create a phospho-defective model. No significant change in tau phosphorylation was observed in the hippocampus of tau Tg; CRMP2KI mice compared to tau Tg littermates. However, when Aβ25-35 oligomers were injected into the hippocampus, tau phosphorylation was significantly reduced in Aβ-injected tau Tg; CRMP2KI mice compared to Aβ-injected tau Tg controls. These findings suggest that CRMP2 phosphorylation at Ser522 promotes Aβ-induced tau phosphorylation in this mouse model of AD.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesHippocampusIntercellular Signaling Peptides and ProteinsNerve Tissue ProteinsNeuronstau ProteinsAnimalsDisease Models, AnimalHumansMiceMice, TransgenicPhosphorylationAmyloid beta-Peptidescollapsin response mediator protein-2Intercellular Signaling Peptides and ProteinsNerve Tissue Proteinstau ProteinsAlzheimer’s diseaseAmyloid peptideMicrogliaPhosphorylationTau

Identifiers

PMID39891817
PMCPMC12078411

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.